Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation

PLoS ONE

Volumn 4, Issue 7, 2009, Pages

  Soares, Dinesh C ^a   Barlow, Paul N ^a   Newbery, Helen J ^a   Porteous, David J ^a   Abbott, Catherine M ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AMINO ACID; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 1ALPHA 1; ELONGATION FACTOR 1ALPHA 2; UNCLASSIFIED DRUG; EEF1A1 PROTEIN, HUMAN; EEF1A2 PROTEIN, HUMAN; ELONGATION FACTOR 1;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; GENE CLUSTER; GENETIC VARIABILITY; MOLECULAR MODEL; MUTAGENESIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; RIBOSOME; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING; YEAST; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BINDING SITES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTOR 1; PHOSPHORYLATION; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 68149126140     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006315     Document Type: Article

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